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P81065 (GST_OCHAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase

EC=2.5.1.18
Gene names
Name:gst
OrganismOchrobactrum anthropi
Taxonomic identifier529 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.3

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the GST superfamily. Beta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.132 mM for glutathione Ref.3

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Glutathione S-transferase
PRO_0000185973

Regions

Domain1 – 8181GST N-terminal
Domain87 – 201115GST C-terminal
Region65 – 662Glutathione binding

Sites

Binding site101Glutathione
Binding site351Glutathione
Binding site521Glutathione; via amide nitrogen and carbonyl oxygen
Binding site1051Glutathione

Experimental info

Mutagenesis101C → A: Strongly reduced affinity for glutathione. Reduces enzyme activity by about 50%. Ref.3
Mutagenesis111S → A: Reduced activity.

Secondary structure

............................... 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81065 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 763B2D3DECA21F2D

FASTA20121,739
        10         20         30         40         50         60 
MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG AVPALEVKPG 

        70         80         90        100        110        120 
TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF CSDLHAAFSG LFAPNLSEEA 

       130        140        150        160        170        180 
RAGVIANINR RLGQLEAMLS DKNAYWLGDD FTQPDAYASV IIGWGVGQKL DLSAYPKALK 

       190        200 
LRERVLARPN VQKAFKEEGL N 

« Hide

References

[1]"Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi."
Favaloro B., Tamburro A., Angelucci S., de Luca A., di Ilio C., Rotilio D.
Biochem. J. 335:573-579(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 50-74, MUTAGENESIS.
[2]"Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi."
Favaloro B., Melino S., Petruzzelli R., di Ilio C., Rotilio D.
FEMS Microbiol. Lett. 160:81-86(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25.
[3]"Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site."
Allocati N., Federici L., Masulli M., Favaloro B., Di Ilio C.
Proteins 71:16-23(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y17279 Genomic DNA. Translation: CAA76728.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NTOX-ray2.10A1-201[»]
2PVQX-ray1.80A1-201[»]
ProteinModelPortalP81065.
SMRP81065. Positions 1-201.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13409. GST_N_2. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81065.

Entry information

Entry nameGST_OCHAN
AccessionPrimary (citable) accession number: P81065
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: June 11, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references